ID A0A2P4ZXT0_9HYPO Unreviewed; 552 AA.
AC A0A2P4ZXT0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=TGAM01_v202179 {ECO:0000313|EMBL:PON29071.1};
OS Trichoderma gamsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=398673 {ECO:0000313|EMBL:PON29071.1, ECO:0000313|Proteomes:UP000054821};
RN [1] {ECO:0000313|EMBL:PON29071.1, ECO:0000313|Proteomes:UP000054821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6085 {ECO:0000313|EMBL:PON29071.1,
RC ECO:0000313|Proteomes:UP000054821};
RX PubMed=26893428;
RA Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL Genome Announc. 4:e01747-15(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001311};
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PON29071.1}.
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DR EMBL; JPDN02000005; PON29071.1; -; Genomic_DNA.
DR RefSeq; XP_018666540.1; XM_018800398.1.
DR AlphaFoldDB; A0A2P4ZXT0; -.
DR STRING; 398673.A0A2P4ZXT0; -.
DR GeneID; 29980481; -.
DR OrthoDB; 731186at2759; -.
DR Proteomes; UP000054821; Unassembled WGS sequence.
DR GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR46072:SF11; AMIDASE-RELATED; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR PIRSF; PIRSF001221; Amidase_fungi; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054821}.
FT DOMAIN 76..534
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 208
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT ACT_SITE 232
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
SQ SEQUENCE 552 AA; 60403 MW; FF543D885078EA71 CRC64;
MSQAAWQDIA HRKRAERDSK IPAEWRISLT SEIGRPIDYL ARCGILTERD LALTDPTHDA
TDLLSQLYSG KVTVEDVVRA FCKRAAVAQQ LTNCLTEIMF SEAIDRAKWL DAEYEKRGKQ
PVGPLHGLPI SVKDMFHIKG YDSSIGTASL CFRPARTTSQ AVQILLDAGC VIIAKTTVPQ
TVLTADTDSI VFGRTINPYN AELTAGGSSG GEGALIAMGG SALGLGSDGG GSIRIPAAMC
GVVGYKPSAY RVPIDGQRII GKGIFGITSL VSPMVSGFLA RSVRDTRLAA KVMSDAKPWD
GSPFIYPHPW VGLSCPSKPR IGVWLKADDL HFHPPVARGL RLACDRLKRA GYEIVELSPP
PFQKASRLAQ QLAEVLDLSY MRKLLESEPH TEIVKATGLI TPKSAPPEFS IEYLHEMNYQ
VARLAMQMKR MWNVDGGKQL DAILFVTAPH TALPFDKFIW LGLTSIFNML DWSSISIPLN
EVVDKKVDTA VVPPKNYLSE LDASIQKLYD AEKFHGLPLA VQLIGQRFED EKLLAVAEEI
APILASRGQS RL
//
